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Database: UniProt
Entry: A0A1C6T0J2_9ACTN
LinkDB: A0A1C6T0J2_9ACTN
Original site: A0A1C6T0J2_9ACTN 
ID   A0A1C6T0J2_9ACTN        Unreviewed;       338 AA.
AC   A0A1C6T0J2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Pyruvate dehydrogenase E1 component beta subunit {ECO:0000313|EMBL:SCL35344.1};
GN   ORFNames=GA0070616_5203 {ECO:0000313|EMBL:SCL35344.1};
OS   Micromonospora nigra.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=145857 {ECO:0000313|EMBL:SCL35344.1, ECO:0000313|Proteomes:UP000199699};
RN   [1] {ECO:0000313|EMBL:SCL35344.1, ECO:0000313|Proteomes:UP000199699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43818 {ECO:0000313|EMBL:SCL35344.1,
RC   ECO:0000313|Proteomes:UP000199699};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FMHT01000003; SCL35344.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6T0J2; -.
DR   STRING; 145857.GA0070616_5203; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000199699; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:SCL35344.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199699}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   338 AA;  36403 MW;  AE38C130EA27E0F0 CRC64;
     MATMTMAKAL NAALADALLD DERVVVFGED VGQLGGVFRI TDGLQARFGD KRCFDTPLAE
     AGIVGFAVGL AMSGLRPVVE MQFDAFAYPA FEQIASHVAK LRNRTRGALS VPMVIRVPYA
     GGIGGVEHHC DSSEAYYAHT PGLKVVTPAT VDDAYSLLRE AIDDPDPVIF MEPKKLYFTS
     AEASLPARTE PFGRAVVRRP GRDATLVAYG PAVPVALEAA EAAREEGWDL EVVDIRTIVP
     FDDATVVESV RRTGRCVVVQ EAQGFAGVGA EIAARVQERC FHALHAPVLR VSGLDIPYPA
     PMLEHTHLPS VDRVLDTVAR LQWDDQPDGR WLAEGAAA
//
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